|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
4-522 |
0e+00 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 969.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 4 QIKVSEVSSILRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQ 83
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 84 IKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIG 163
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEE-RRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 164 RGQRELIIGDRQTGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQ 243
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQK-----GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 244 YFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevaremn 323
Cdd:COG0056 236 YIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAK------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 324 dlpesMRDKvKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKK 403
Cdd:COG0056 304 -----LSDE-LGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 404 VAGTLKIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFE 483
Cdd:COG0056 378 VAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFE 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1489380151 484 ARFLQELRTSHQrDVLDVLK-TGVINDEIRGILEKTAKEL 522
Cdd:COG0056 458 KELLEYLRAKHP-DLLKEIReTGKLDDEIEEKLKAAIEEF 496
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
4-522 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 955.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 4 QIKVSEVSSILRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQ 83
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 84 IKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIG 163
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATE-TRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 164 RGQRELIIGDRQTGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQ 243
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQK-----GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 244 YFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevaremn 323
Cdd:PRK09281 236 YLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAK------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 324 dlpesMRDKvKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKK 403
Cdd:PRK09281 304 -----LSDE-LGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 404 VAGTLKIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFE 483
Cdd:PRK09281 378 VAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFE 457
|
490 500 510
....*....|....*....|....*....|....*....
gi 1489380151 484 ARFLQELRTSHQRDVLDVLKTGVINDEIRGILEKTAKEL 522
Cdd:PRK09281 458 AELLAYLRSNHADLLEEIRETKDLSDEIEAKLKAAIEEF 496
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
4-522 |
0e+00 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 780.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 4 QIKVSEVSSILRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQ 83
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 84 IKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETCEmPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIG 163
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFS-PVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 164 RGQRELIIGDRQTGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQ 243
Cdd:TIGR00962 160 RGQRELIIGDRQTGKTAVAIDTIINQK-----DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 244 YFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevareMN 323
Cdd:TIGR00962 235 YLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAK----------LN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 324 DlpesmrdkVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKK 403
Cdd:TIGR00962 305 D--------EKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 404 VAGTLKIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFE 483
Cdd:TIGR00962 377 VAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFE 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 1489380151 484 ARFLQELRTSHQRDVLDVLKTGVINDEIRGILEKTAKEL 522
Cdd:TIGR00962 457 QALLAYLDANHPDILEEINTTKKLTEELEAKLKEALKNF 495
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
9-522 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 741.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 9 EVSSILRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGD 88
Cdd:PRK13343 7 EWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 89 TVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEiLGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRE 168
Cdd:PRK13343 87 EVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGP-LQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 169 LIIGDRQTGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPF 248
Cdd:PRK13343 166 LIIGDRQTGKTAIAIDAIINQK-----DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 249 AGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevareMNDLpes 328
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAK----------LSPE--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 329 mrdkvKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTL 408
Cdd:PRK13343 308 -----LGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 409 KIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFEARFLQ 488
Cdd:PRK13343 383 RLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLE 462
|
490 500 510
....*....|....*....|....*....|....
gi 1489380151 489 ELRTSHQRDVLDVLKTGVINDEIRGILEKTAKEL 522
Cdd:PRK13343 463 KLDARFAALSLALESPRELDEAWLAALEEILREA 496
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
25-521 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 722.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 25 IKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEG 104
Cdd:CHL00059 2 VKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 105 MIGRVIDPLGNPIDGKGEIlgETCEMPL-ERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAI 183
Cdd:CHL00059 82 YLGRVVNALAKPIDGKGEI--SASESRLiESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 184 DTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRH 263
Cdd:CHL00059 160 DTILNQK-----GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 264 ALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIINQpevaremndlpesmrdkvKGGGSLTALP 343
Cdd:CHL00059 235 TLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQ------------------LGEGSMTALP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 344 IIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTLKIDQAQFRELESFSK 423
Cdd:CHL00059 297 IVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 424 FGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFEARFLQELRTSHQRDVLDVLK 503
Cdd:CHL00059 377 FASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISS 456
|
490
....*....|....*...
gi 1489380151 504 TGVINDEIRGILEKTAKE 521
Cdd:CHL00059 457 TKTFTEEAEALLKEAIQE 474
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
14-520 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 565.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 14 LRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRT 93
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 94 GRIASIDVSEGMIGRVIDPLGNPIDGKGEiLGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGD 173
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGP-LASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 174 RQTGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAI 253
Cdd:TIGR03324 171 RQTGKTAIAIDTILNQK-----GRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 254 GEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIInqpevaremndlpesmrdKV 333
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLN------------------EE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 334 KGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTLKIDQA 413
Cdd:TIGR03324 308 LGGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 414 QFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVHEFEARfLQELRTS 493
Cdd:TIGR03324 388 QFEELETFARFGARLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESA-IRAAVTS 466
|
490 500
....*....|....*....|....*...
gi 1489380151 494 HQRDVLDVLKTG-VINDEIRGILEKTAK 520
Cdd:TIGR03324 467 LPADLRERLQSGkKLSDEDREQILDIAR 494
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-393 |
0e+00 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 556.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 96 IASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQ 175
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKE-RRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 176 TGKTSIAIDTIINQRsnyeaGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGE 255
Cdd:cd01132 80 TGKTAIAIDTIINQK-----GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 256 YFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevareMNDlpesmrdkVKG 335
Cdd:cd01132 155 YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAK----------LSD--------ELG 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489380151 336 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVG 393
Cdd:cd01132 217 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
63-483 |
1.69e-118 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 360.89 E-value: 1.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 63 AIVMNLEEDN-VGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPID------GKGEILGETCEMPLERK 135
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 136 APGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDTIINQ-RSNYE--AGNPVYCIYVAIGQKGST 212
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvRINQQilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 213 VAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGRE 292
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 293 AYPGDIFYLHSRLLERAAkiinqpevaremndlpesMRDKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLET 372
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAA------------------MLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDT 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 373 DLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTLKIDQAQFRELESFSKFGGEMDAVTAFtidKGQKNTQLLIQPQys 452
Cdd:PTZ00185 382 KLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVPMI---RGARFVALFNQKN-- 456
|
410 420 430
....*....|....*....|....*....|.
gi 1489380151 453 PMPVEEQISILYCGTQGLLKEVPLDKVHEFE 483
Cdd:PTZ00185 457 PSFFMNALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
152-390 |
6.62e-111 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 328.16 E-value: 6.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 152 GIKAVDAMIPIGRGQRELIIGDRQTGKTSIAiDTIINQRSNYeagnpvYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIV 231
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD------VVVYALIGERGREVREFIEELLGSGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 232 VSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAK 311
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489380151 312 IINqpevaremndlpesmrdkvkGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVS 390
Cdd:pfam00006 154 VKG--------------------KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
36-453 |
4.74e-103 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 318.84 E-value: 4.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 36 VSDGVARIYGLDNAEANELLQFDNGME--AIVMNLEEDNvgAVLL--GPTDQIKEGDTVKRTGRIASIDVSEGMIGRVID 111
Cdd:PRK07165 8 IFDYIVEVKGEYDYQQNQFFTLKNNPNvkAFVISATEDK--AYLLinNEKGKIKINDELIELNNTNKVKTSKEYFGKIID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 112 PLGNPIDGKGEIlgETCEMPLERKAP------GVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDT 185
Cdd:PRK07165 86 IDGNIIYPEAQN--PLSKKFLPNTSSifnlahGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 186 IINQRSnyeagNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSAtASDPAAMQYFAPFAGAAIGE---YFRDsgr 262
Cdd:PRK07165 164 IINQKN-----TNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 263 hALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIinqpevaremndlpesmrdkvKGGGSLTAL 342
Cdd:PRK07165 235 -VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---------------------KNRKTITAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 343 PIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTL-KIDQAQFRELEsF 421
Cdd:PRK07165 293 PILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEIsKIYRAYKRQLK-L 371
|
410 420 430
....*....|....*....|....*....|..
gi 1489380151 422 SKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSP 453
Cdd:PRK07165 372 SMLDYDLNKETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
98-392 |
8.65e-102 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 307.07 E-value: 8.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 98 SIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTG 177
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQ-RRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 178 KTSIAIDTIINQRSNyEAGnpvYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYF 257
Cdd:cd19476 80 KTVLAMQLARNQAKA-HAG---VVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 258 RDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIINqpevaremndlpesmrdkvkGGG 337
Cdd:cd19476 156 RDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--------------------GGG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1489380151 338 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRV 392
Cdd:cd19476 216 SITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
397-521 |
5.96e-51 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 169.93 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 397 QLKAMKKVAGTLKIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPL 476
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1489380151 477 DKVHEFEARFLQELRTSHqRDVLDVL-KTGVINDEIRGILEKTAKE 521
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNH-PEILEEIeETKKLSDELEEKLKEAIEE 125
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
401-522 |
7.92e-51 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 169.85 E-value: 7.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 401 MKKVAGTLKIDQAQFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQGLLKEVPLDKVH 480
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489380151 481 EFEARFLQELRTSHQrDVLD-VLKTGVINDEIRGILEKTAKEL 522
Cdd:cd18113 81 EFEKELLEYLRSNHP-DLLEeIEKTKKLSDELEEKLKEAIEEF 122
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
98-392 |
1.10e-50 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 174.29 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 98 SIDVSEGMIGRVIDPLGNPIDGKGEiLGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTG 177
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGL-PDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 178 KTsiaidTIINQRSNYeAGNPVYCIyVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYF 257
Cdd:cd01136 80 KS-----TLLGMIARN-TDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 258 RDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIINqpevaremndlpesmrdkvkggG 337
Cdd:cd01136 153 RDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----------------------G 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1489380151 338 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRV 392
Cdd:cd01136 211 SITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
14-420 |
5.97e-47 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 169.06 E-value: 5.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 14 LRQQLEGIHTsikLEEVGTVLQVSDGVARIYGLDnAEANELLQFDNG----MEAIVMNLEEDNVGAVLLGPTDQIKEGDT 89
Cdd:COG1157 7 LLARLEELPP---VRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETAdgrpVLAEVVGFRGDRVLLMPLGDLEGISPGAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 90 VKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRel 169
Cdd:COG1157 83 VVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE-RRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 170 iIGdr---qtGKTS----IA----IDTIInqrsnyeagnpvyciyVA-IGQKGSTVAALV-NTLQEKGaMDYTIVVSATA 236
Cdd:COG1157 160 -IGifagsgvGKSTllgmIArnteADVNV----------------IAlIGERGREVREFIeDDLGEEG-LARSVVVVATS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 237 SDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqp 316
Cdd:COG1157 222 DEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 317 evaremndlpesmrdkvKGGGSLTAL------------PIIETqagdvsayiptnVISITDGQIFLETDLFNQGNRPAIN 384
Cdd:COG1157 297 -----------------GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAID 347
|
410 420 430
....*....|....*....|....*....|....*..
gi 1489380151 385 VGISVSRVggnaqlkaMKKVAGTLKIDQAQ-FRELES 420
Cdd:COG1157 348 VLASISRV--------MPDIVSPEHRALARrLRRLLA 376
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
58-420 |
2.83e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.42 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 58 DNGMEAIVMNLEEDNVgavLLGPTDQIKE---GDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLER 134
Cdd:PRK07721 52 DKAIKAEVVGFKDEHV---LLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLA-PVSTDQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 135 KAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAidTIINQRSNYEAGnpvycIYVAIGQKGSTVA 214
Cdd:PRK07721 128 DPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLM--GMIARNTSADLN-----VIALIGERGREVR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 215 ALV-NTLQEKGaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREA 293
Cdd:PRK07721 201 EFIeRDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 294 YPGDIFYLHSRLLERAAkiinqpevaremndlpesmrdkVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETD 373
Cdd:PRK07721 280 YTPSVFAILPKLLERTG----------------------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQ 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1489380151 374 LFNQGNRPAINVGISVSRVggnaqlkaMKKVAGTLKIDQAQ-FRELES 420
Cdd:PRK07721 338 LANKGQYPAINVLKSVSRV--------MNHIVSPEHKEAANrFRELLS 377
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-425 |
2.97e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 153.82 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 7 VSEVSSILRQQL-------EGIHTSIKLEEVG-TVLQVSdgvariygLDNAEANELLQFD-NGMEAIVMNLEEDNVgavL 77
Cdd:PRK06820 6 IARLTPRLQQQLtrpsappEGLRYRGPIVEIGpTLLRAS--------LPGVAQGELCRIEpQGMLAEVVSIEQEMA---L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 78 LGP---TDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGkGEILGETCEmPLERKAPGVIFRQPVNEPLQTGIK 154
Cdd:PRK06820 75 LSPfasSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 155 AVDAMIPIGRGQRELIIGDRQTGKTSIAidtiinqrSNYEAGNPVYCIYVA-IGQKGSTVAALVNTLQEKGAMDYTIVVS 233
Cdd:PRK06820 153 AIDGILSCGEGQRIGIFAAAGVGKSTLL--------GMLCADSAADVMVLAlIGERGREVREFLEQVLTPEARARTVVVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 234 ATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkii 313
Cdd:PRK06820 225 ATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 314 nqpevaremndlPESMrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVG 393
Cdd:PRK06820 302 ------------NSDR-------GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
410 420 430
....*....|....*....|....*....|..
gi 1489380151 394 GNAQLKAMKKVAGTLKIDQAQFRELESFSKFG 425
Cdd:PRK06820 363 PQIVSAGQLAMAQKLRRMLACYQEIELLVRVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
14-409 |
8.12e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 152.53 E-value: 8.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 14 LRQQLEGIHTSIKLeevGTVLQVSDGVARIYGLDNA-------EANELLQFDNGMeaiVMNLEEDNVGAVLLGPTDQIKE 86
Cdd:PRK08472 6 LKNKLQKFNLSPRF---GSITKISPTIIEADGLNPSvgdivkiESSDNGKECLGM---VVVIEKEQFGISPFSFIEGFKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 87 GDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQ 166
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYER-YAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 167 RELIIGDRQTGKTSIaIDTIINqrsNYEAgnPVYCIYVaIGQKGSTVAALVNTlQEKGAMDYTIVVSATASDPAAMQYFA 246
Cdd:PRK08472 159 KLGIFAGSGVGKSTL-MGMIVK---GCLA--PIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 247 PFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevaremndlp 326
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAG---------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 327 esmrdKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAG 406
Cdd:PRK08472 295 -----KEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAAR 369
|
...
gi 1489380151 407 TLK 409
Cdd:PRK08472 370 KFK 372
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
11-468 |
2.28e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 145.67 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 11 SSILRQQLEGIHTSIKLEEVGTVLQVSDGVAR--IYGLDNAEANELLQFDN--GMEAIVMNLEEDNVGAVLLGPTDQIKE 86
Cdd:PRK06936 5 DYIPHHLRHAIVGSRLIQIRGRVTQVTGTILKavVPGVRIGELCYLRNPDNslSLQAEVIGFAQHQALLTPLGEMYGISS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 87 GDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGkGEILGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQ 166
Cdd:PRK06936 85 NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDG-GHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 167 RELIIGDRQTGKTSIAIDTIINQRSNYeagnpvyCIYVAIGQKGSTVAALV-NTLQEKGaMDYTIVVSATASDPAAMQYF 245
Cdd:PRK06936 164 RMGIFAAAGGGKSTLLASLIRSAEVDV-------TVLALIGERGREVREFIeSDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 246 APFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevaremndl 325
Cdd:PRK06936 236 AGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 326 pesMRDKvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVA 405
Cdd:PRK06936 301 ---QSDK----GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489380151 406 GTLKIDQAQFRELESFSKFG----GEmDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGTQ 468
Cdd:PRK06936 374 GRLRELLAKYEEVELLLQIGeyqkGQ-DKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-425 |
7.58e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 141.63 E-value: 7.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 63 AIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGeiLGETCEMPLERKAPGVIFR 142
Cdd:PRK07594 55 AEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVCWKDYDAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 143 QPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTsiaidTIINQRSNyeAGNPVYCIYVAIGQKGSTVAALVNTLQE 222
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS-----TLLAMLCN--APDADSNVLVLIGERGREVREFIDFTLS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 223 KGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLH 302
Cdd:PRK07594 206 EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 303 SRLLERAAkiinqpevaremndlpesMRDKvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPA 382
Cdd:PRK07594 286 PRLLERTG------------------MGEK----GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPA 343
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1489380151 383 INVGISVSRVGGNAQLKAMKKVAGTLKIDQAQFRELESFSKFG 425
Cdd:PRK07594 344 IDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
31-401 |
1.48e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 140.90 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 31 GTVLQVSDGVARIYGL-DNAEANELLQFDNGMEAI---VMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRiASIDVSEGMI 106
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRADGGTHlgeVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 107 GRVIDPLGNPIDGKGEILGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSI----- 181
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 182 ---AIDTIInqrsnyeagnpvyciyVA-IGQKGSTVAA-LVNTLQekGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEY 256
Cdd:PRK06002 187 radAFDTVV----------------IAlVGERGREVREfLEDTLA--DNLKKAVAVVATSDESPMMRRLAPLTATAIAEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 257 FRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevaremndlPESmrdkvKGG 336
Cdd:PRK06002 249 FRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG---------------PGA-----EGG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489380151 337 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNA----------QLKAM 401
Cdd:PRK06002 309 GSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAwtpeqrklvsRLKSM 383
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
27-425 |
2.09e-36 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 140.29 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 27 LEEVGTVLQVSdGVARIYGldnaEANELLQFDNGM--EAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEG 104
Cdd:PRK09099 29 VEVIGTLLRVS-GLDVTLG----ELCELRQRDGTLlqRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 105 MIGRVIDPLGNPIDGKGEILGETCEmPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTsiaid 184
Cdd:PRK09099 104 LLGRVIDGLGEPIDGGGPLDCDELV-PVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 185 TIINQRSNYEAGNpVYCIyVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATaSDPAAMQYF-APFAGAAIGEYFRDSGRH 263
Cdd:PRK09099 178 TLMGMFARGTQCD-VNVI-ALIGERGREVREFIELILGEDGMARSVVVCAT-SDRSSIERAkAAYVATAIAEYFRDRGLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 264 ALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevareMNDLpesmrdkvkggGSLTALP 343
Cdd:PRK09099 255 VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----------MGET-----------GSITALY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 344 IIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTLKIDQAQFRELESFSK 423
Cdd:PRK09099 313 TVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
..
gi 1489380151 424 FG 425
Cdd:PRK09099 393 VG 394
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
90-464 |
3.76e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 136.66 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 90 VKRTGRIASIDVSEGMIGRVIDPLGN---PIDGKGEILGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQ 166
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 167 RELIIGDRQTGKTSIaIDTIINQrsnyeAGNPVYCIYVaIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFA 246
Cdd:PRK08149 153 RMGIFASAGCGKTSL-MNMLIEH-----SEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 247 PFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKIINqpevaremndlp 326
Cdd:PRK08149 226 ALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA------------ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 327 esmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVGGNAQLKAMKKVAG 406
Cdd:PRK08149 294 ----------GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAA 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489380151 407 TLKIDQAQFRELESFSKFG----GEmDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILY 464
Cdd:PRK08149 364 AFRKLLTRLEELQLFIDLGeyrrGE-NADNDRAMDKRPALEAFLKQDVAEKSSFSDTLERLN 424
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
96-406 |
7.82e-35 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 131.96 E-value: 7.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 96 IASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQ 175
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPED-YLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 176 TGKTSIAIdTIINQRSNYEAGNPVYCIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGE 255
Cdd:cd01135 80 LPHNELAA-QIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 256 YFR-DSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGdifYLHSRL---LERAAKIINQPevaremndlpesmrd 331
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGRK--------------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489380151 332 kvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRVggnaqlkaMKKVAG 406
Cdd:cd01135 221 -----GSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
54-420 |
4.21e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 134.06 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 54 LLQFDNG-MEAIVMNLEEDNVgavLLGPTDQIK---EGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcE 129
Cdd:PRK08972 51 SIETMAGeLEAEVVGFDGDLL---YLMPIEELRgvlPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQ-R 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 130 MPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKtSIAIDTIINqrsnyeaGNPVYCIYVA-IGQ 208
Cdd:PRK08972 127 ASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK-SVLLGMMTR-------GTTADVIVVGlVGE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 209 KGSTVAALV-NTLQEKGaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRR 287
Cdd:PRK08972 199 RGREVKEFIeEILGEEG-RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 288 PSGREAYPGDIFYLHSRLLERAAkiiNQPEvaremndlpesmrdkvkGGGSLTALPIIETQAGDVSAYIPTNVISITDGQ 367
Cdd:PRK08972 278 PPATKGYPPSVFAKLPALVERAG---NGGP-----------------GQGSITAFYTVLTEGDDLQDPIADASRAILDGH 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489380151 368 IFLETDLFNQGNRPAINVGISVSRVG----GNAQLKAMKKVAGTLKIDQaQFRELES 420
Cdd:PRK08972 338 IVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRVKQVYSLYQ-QNRDLIS 393
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
65-391 |
2.76e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 131.87 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 65 VMNLEEDNVGAVLLGPTDQIKEGDT-VKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGEtCEMPLERKAPGVIFRQ 143
Cdd:PRK04196 43 VLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE-KRLDINGAPINPVARE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 144 PVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDtIINQRSNYEAGNPVYCIYVAIGQKGSTVAALVNTLQEK 223
Cdd:PRK04196 122 YPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ-IARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEET 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 224 GAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFR-DSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGdifYLH 302
Cdd:PRK04196 201 GALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 303 SRL---LERAAKIINQPevaremndlpesmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGN 379
Cdd:PRK04196 278 TDLatiYERAGRIKGKK--------------------GSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGI 337
|
330
....*....|..
gi 1489380151 380 RPAINVGISVSR 391
Cdd:PRK04196 338 YPPIDVLPSLSR 349
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
61-450 |
2.97e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 131.78 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 61 MEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGVI 140
Cdd:PRK05688 65 VEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAED-WVPMDGPTINPL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 141 FRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTsiaidTIINQRSNYEAGNpvycIYVA--IGQKGSTVAALV- 217
Cdd:PRK05688 144 NRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKS-----VLLGMMTRFTEAD----IIVVglIGERGREVKEFIe 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 218 NTLQEKGaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGD 297
Cdd:PRK05688 215 HILGEEG-LKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 298 IFYLHSRLLERAAkiinqpevaremndlpesmrDKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQ 377
Cdd:PRK05688 294 VFAKLPKLVERAG--------------------NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEE 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489380151 378 GNRPAINVGISVSRVggnaqlkaMKKVAGTLKIDQAQ-FRELESFSKFGGEMDAVTAFTiDKGQKNTQLLIQPQ 450
Cdd:PRK05688 354 GHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSRDLISVGAYV-AGGDPETDLAIARF 418
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
14-391 |
8.43e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 127.33 E-value: 8.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 14 LRQQLEGIHTSIKLEEVGTVLQVSDGVARIYGLdNAEANELLQF----DNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDT 89
Cdd:PRK05922 4 LQEEKLLIHQWQPYRECGLLSRVSGNLLEAQGL-SACLGELCQIslskSPPILAEVIGFHNRTTLLMSLSPIHYVALGAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 90 VKRTGRIASIDVSEGMIGRVIDPLGNPIDGKgEILGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQREL 169
Cdd:PRK05922 83 VLPLRRPPSLHLSDHLLGRVLDGFGNPLDGK-EQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 170 IIGDRQTGKTSIAIDTIINQRSNYEagnpvycIYVAIGQKGSTVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFA 249
Cdd:PRK05922 162 VFSEPGSGKSSLLSTIAKGSKSTIN-------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 250 GAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAKiinqpevaremNDlpesm 329
Cdd:PRK05922 235 AMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-----------ND----- 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489380151 330 rdkvkgGGSLTALPIIETQAGDVSAYIPTnVISITDGQIFLEtdlfNQGN---RPAINVGISVSR 391
Cdd:PRK05922 299 ------KGSITALYAILHYPNHPDIFTDY-LKSLLDGHFFLT----PQGKalaSPPIDILTSLSR 352
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
101-463 |
1.34e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 126.54 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 101 VSEGMIGRVIDPLGNPIDGKGEILGETcemPLERKAPGV--IFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGK 178
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGST---PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 179 TsiaidTIINQRSNYEAGNPVycIYVAIGQKGSTVAALV-NTLQEKGaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYF 257
Cdd:PRK07196 169 S-----VLLGMITRYTQADVV--VVGLIGERGREVKEFIeHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 258 RDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevaremndlpesmrdKVKGGG 337
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---------------------NSSGNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 338 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSR----VGGNAQLKAMKKVAGTLKiDQA 413
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYM 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1489380151 414 QFRELESFSKFGGEMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISIL 463
Cdd:PRK07196 379 AIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEVGHPALFSASVEQL 428
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
29-95 |
4.62e-31 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 114.47 E-value: 4.62e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489380151 29 EVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGR 95
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
75-391 |
2.12e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.17 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 75 AVLL--GPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETCEMPLERKAPGVIFRQPVNEPLQTG 152
Cdd:PRK08927 66 ALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 153 IKAVDAMIPIGRGQRELIIGDRQTGKTSI--------AIDTIInqrsnyeagnpvycIYVaIGQKGSTVAALV-NTLQEK 223
Cdd:PRK08927 146 VRALNTFLTCCRGQRMGIFAGSGVGKSVLlsmlarnaDADVSV--------------IGL-IGERGREVQEFLqDDLGPE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 224 GaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHS 303
Cdd:PRK08927 211 G-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 304 RLLERAAkiinqPEVAREmndlpesmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAI 383
Cdd:PRK08927 290 RLLERAG-----PGPIGE---------------GTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAI 349
|
....*...
gi 1489380151 384 NVGISVSR 391
Cdd:PRK08927 350 NVLKSVSR 357
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
68-484 |
4.96e-28 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 116.74 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 68 LEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEIlGETCEMPLERKAPGVIFRQPVNE 147
Cdd:TIGR01039 47 LGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPI-PAKERWPIHRKAPSFEEQSTKVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 148 PLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDTIINQRSNYEAgnpvYCIYVAIGQKGSTVAALVNTLQEKGAMD 227
Cdd:TIGR01039 126 ILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG----YSVFAGVGERTREGNDLYHEMKESGVID 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 228 YTIVVSATASDPAAMQYFAPFAGAAIGEYFRD-SGRHALVVYDDLSKQAVAYREVSLILRRpsgreaYPGDIFYlhsrll 306
Cdd:TIGR01039 202 KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGR------MPSAVGY------ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 307 eraakiinQPEVAREMNDLPEsmRDKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVG 386
Cdd:TIGR01039 270 --------QPTLATEMGELQE--RITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 387 ISVSR-----VGGNAQLKAMKKVAGTLKidqaQFRELESFSKFGGeMDAVT---AFTIDKGQKNTQLLIQpqysPMPVEE 458
Cdd:TIGR01039 340 DSTSRlldpsVVGEEHYDVARGVQQILQ----RYKELQDIIAILG-MDELSeedKLTVERARRIQRFLSQ----PFFVAE 410
|
410 420
....*....|....*....|....*..
gi 1489380151 459 QISilycGTQGllKEVPL-DKVHEFEA 484
Cdd:TIGR01039 411 VFT----GQPG--KYVPLkDTIRGFKE 431
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
89-401 |
5.60e-25 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 107.89 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 89 TVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETCempLErkapgvIFRQPVN--------EPLQTGIKAVDAMI 160
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDY---LD------INGQPINpyariypeEMIQTGISAIDVMN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 161 PIGRGQRELIIGD-------------RQTGKTSIAIDTIINQRSNYEAgnpvyCIYVAIGQKGSTVAALVNTLQEKGAMD 227
Cdd:TIGR01040 137 SIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFA-----IVFAAMGVNMETARFFKQDFEENGSME 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 228 YTIVVSATASDPAAMQYFAPFAGAAIGEYFR-DSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLL 306
Cdd:TIGR01040 212 RVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 307 ERAAKIINQPevaremndlpesmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVG 386
Cdd:TIGR01040 292 ERAGRVEGRN--------------------GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVL 351
|
330
....*....|....*
gi 1489380151 387 ISVSRVGGNAQLKAM 401
Cdd:TIGR01040 352 PSLSRLMKSAIGEGM 366
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
65-425 |
1.62e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 105.83 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 65 VMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDplgnpidGKGEILGETCEM-PLER---KAPGV- 139
Cdd:PRK06793 57 VIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLS-------ANGEVLNEEAENiPLQKiklDAPPIh 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 140 -IFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDTIINQRSNYEagnpvycIYVAIGQKGSTVAALV- 217
Cdd:PRK06793 130 aFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN-------VISLVGERGREVKDFIr 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 218 NTLQEKGaMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRR-PSGreaypG 296
Cdd:PRK06793 203 KELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKElPIG-----G 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 297 DIFYLHS---RLLERAAKIINqpevaremndlpesmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETD 373
Cdd:PRK06793 277 KTLLMESymkKLLERSGKTQK----------------------GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRE 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1489380151 374 LFNQGNRPAINVGISVSRVGGNAQLKAMKKVAGTLKIDQAQFRELESFSKFG 425
Cdd:PRK06793 335 LATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLG 386
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
105-421 |
8.84e-24 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 104.09 E-value: 8.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 105 MIGRVIDPLGNPIDGKGEilGETCE-MPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTsiai 183
Cdd:PRK07960 116 LLGRVLDGSGKPLDGLPA--PDTGEtGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS---- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 184 dTIINQRSNYEAGNpvyCIYVA-IGQKGSTVAALV-NTLQEKG-AMDYTIVVSATASDPAAMQyfapfaGAA----IGEY 256
Cdd:PRK07960 190 -VLLGMMARYTQAD---VIVVGlIGERGREVKDFIeNILGAEGrARSVVIAAPADVSPLLRMQ------GAAyatrIAED 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 257 FRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGDIFYLHSRLLERAAkiinqpevaremndlpesmrDKVKGG 336
Cdd:PRK07960 260 FRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--------------------NGISGG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 337 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRvggnaqlkAMkkvagTLKIDQAQFR 416
Cdd:PRK07960 320 GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR--------AM-----TALIDEQHYA 386
|
....*
gi 1489380151 417 ELESF 421
Cdd:PRK07960 387 RVRQF 391
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
98-391 |
6.82e-22 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 95.72 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 98 SIDVSEGMIGRVIDPLGNPIdgkgEILGETC-----------EMPLERKAPgVIFRQPVNEPLQTGIKAVDAMIPIGRGQ 166
Cdd:cd01134 3 SVELGPGLLGSIFDGIQRPL----EVIAETGsifiprgvnvqRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 167 RELIIGDRQTGKTsiaidTIINQRSNYEAGNPVycIYVAIGQKGSTVA-------ALVNTLQEKGAMDYTIVVSATASDP 239
Cdd:cd01134 78 TAAIPGPFGCGKT-----VISQSLSKWSNSDVV--IYVGCGERGNEMAevleefpELKDPITGESLMERTVLIANTSNMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 240 AAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGREAYPGdifYLHSRL---LERAAKIINQP 316
Cdd:cd01134 151 VAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVRCLG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489380151 317 EVAREmndlpesmrdkvkggGSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LETDLFNQGNRPAINVGISVSR 391
Cdd:cd01134 228 SPGRE---------------GSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
58-373 |
2.36e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.48 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 58 DNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETCEM------P 131
Cdd:PRK02118 35 DGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPIEIggpsvnP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 132 LERKAPgvifrqpvNEPLQTGIKAVDAMIPIGRGQRELIIGDrqTGKTSIAIDTIINQRSNYEAgnpvyCIYVAIGQKGS 211
Cdd:PRK02118 115 VKRIVP--------REMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALLARIALQAEADI-----IILGGMGLTFD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 212 TVAALVNTLQEKGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFR-DSGRHALVVYDDLSKQAVAYREVSLILRR-PS 289
Cdd:PRK02118 180 DYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQiPS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 290 GReAYPGDifyLHSRLLERAAKIINqpevaremndlpesmrdkVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIF 369
Cdd:PRK02118 260 NR-GYPGS---LYSDLASRYEKAVD------------------FEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFY 317
|
....
gi 1489380151 370 LETD 373
Cdd:PRK02118 318 LRRG 321
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-392 |
9.62e-16 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 77.65 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 98 SIDVSEGMIGRVIDPLGNPIDGKGEIlGETCEMPLERKAPGVIFRQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTG 177
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPI-KAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 178 KTSIaIDTIINqrsNYEAGNPVYCIYVAIGQKGSTVAALVNTLQEKG-----AMDYTIVVSATASDPAAMQYFAPFAGAA 252
Cdd:cd01133 80 KTVL-IMELIN---NIAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 253 IGEYFRDS-GRHALVVYDDLSKQAVAYREVSLIL-RRPSgREAYpgdifylhsrlleraakiinQPEVAREMNDLPEsmR 330
Cdd:cd01133 156 MAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLgRIPS-AVGY--------------------QPTLATEMGSLQE--R 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489380151 331 DKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFNQGNRPAINVGISVSRV 392
Cdd:cd01133 213 ITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
28-94 |
8.37e-15 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 69.11 E-value: 8.37e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489380151 28 EEVGTVLQVSDGVARIYGLDNAEANELLQFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTG 94
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
202-384 |
3.78e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 65.81 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 202 IYVAIGQKGSTVAALVNTLQE-------KGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQ 274
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 275 AVAYREVSLILRRPSGREAYPGdifYLHSRL---LERAAKIINQPEVAREmndlpesmrdkvkggGSLTALPIIETQAGD 351
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVVTLGSDYRV---------------GSVSVIGAVSPPGGD 827
|
170 180 190
....*....|....*....|....*....|...
gi 1489380151 352 VSAYIPTNVISITDGQIFLETDLFNQGNRPAIN 384
Cdd:PRK14698 828 FSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
65-419 |
5.35e-11 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 64.68 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 65 VMNLEEDN-VGAVLLGPTDQIKEGDTVKRTGRIASIDVSEGMIGRVIDPLGNPIDGKGEILGETcEMPLERKAPGviFRQ 143
Cdd:CHL00060 61 VQQLLGNNrVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRT-TSPIHRSAPA--FIQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 144 PVNEP--LQTGIKAVDAMIPIGRGQRELIIGDRQTGKTSIAIDTIIN---------------QRSnyEAGNPVYciyvaI 206
Cdd:CHL00060 138 LDTKLsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgERT--REGNDLY-----M 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 207 GQKGSTVAALVNTLQEKGAMDYtivvsATASDPAAMQYFAPFAGAAIGEYFRDSGRH-ALVVYDDLSKQAVAYREVSLIL 285
Cdd:CHL00060 211 EMKESGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 286 -RRPSGreaypgdIFYlhsrlleraakiinQPEVAREMNDLPE---SMRDkvkggGSLTALPIIETQAGDVSAYIPTNVI 361
Cdd:CHL00060 286 gRMPSA-------VGY--------------QPTLSTEMGSLQEritSTKE-----GSITSIQAVYVPADDLTDPAPATTF 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489380151 362 SITDGQIFLETDLFNQGNRPAINVGISVS-----RVGGNAQLKAMKKVAGTLKidqaQFRELE 419
Cdd:CHL00060 340 AHLDATTVLSRGLAAKGIYPAVDPLDSTStmlqpRIVGEEHYETAQRVKQTLQ----RYKELQ 398
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
142-314 |
6.99e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 64.80 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 142 RQPVNEPLQTGIKAVDAMIPIGRGQRELIIGDRQTGKTsiaidTIINQRSNYEAGNPVycIYVAIGQKGSTVaalVNTLQ 221
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-----VTQHQLAKWADADIV--IYVGCGERGNEM---TEVLE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489380151 222 E----------KGAMDYTIVVSATASDPAAMQYFAPFAGAAIGEYFRDSGRHALVVYDDLSKQAVAYREVSLILRRPSGR 291
Cdd:PRK04192 274 EfpelidpktgRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGE 353
|
170 180
....*....|....*....|....*.
gi 1489380151 292 EAYPGdifYLHSRL---LERAAKIIN 314
Cdd:PRK04192 354 EGYPA---YLASRLaefYERAGRVKT 376
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
401-467 |
1.54e-10 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 57.07 E-value: 1.54e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489380151 401 MKKVAGTLKIDQAQFRELESFSKFGG--EMDAVTAFTIDKGQKNTQLLIQPQYSPMPVEEQISILYCGT 467
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGddALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
31-95 |
3.28e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 39.22 E-value: 3.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489380151 31 GTVLQVSDGVARIYGLDNAEANELL-------QFDNGMEAIVMNLEEDNVGAVLLGPTDQIKEGDTVKRTGR 95
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCeiergdgNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
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|